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Human aspartylglucosaminidase belongs to the newly recognized structural superfamily of Ntn aminohydrolases, which are characterized by the use of the side chain of the N-terminal amino acid as the nucleophile in catalysis.
The new refinement of GroEL sharpens the boundary between known and unknown regions of the structure, and raises questions about the treatment of ambiguity in structure determination.
Protein tyrosine phosphatases (PTPs) are a family of signal transduction enzymes that dephosphorylate phosphotyrosine containing proteins. Structural and kinetic studies provide a molecular understanding of how these enzymes regulate a wide range of intracellular processes.
Measurement of proton uptake in the bacterial photosynthetic reaction centre indicates that the formation of has an electrostatic influence on the protonation of residue Glu-L212 some 17 Å distant from .
An antiparallel DNA decanucleotide displays an unusual crystal structure in which each molecule is linked to a neighbour by base pairs between intertwined, looped strands. The structure suggests a model for the transcription bubble.
